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Database: UniProt/TrEMBL
Entry: A0A095FX67_BURPE
LinkDB: A0A095FX67_BURPE
Original site: A0A095FX67_BURPE 
ID   A0A095FX67_BURPE        Unreviewed;       994 AA.
AC   A0A095FX67;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-NOV-2017, entry version 24.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=DP46_697 {ECO:0000313|EMBL:AIO86419.1};
OS   Burkholderia pseudomallei (Pseudomonas pseudomallei).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=28450 {ECO:0000313|EMBL:AIO86419.1};
RN   [1] {ECO:0000313|EMBL:AIO86419.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=9 {ECO:0000313|EMBL:AIO86419.1};
RA   Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA   Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S.,
RA   Gu W., Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA   Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA   Scholz M.B., Teshima H., Xu Y.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946753}.
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DR   EMBL; CP008755; AIO86419.1; -; Genomic_DNA.
DR   RefSeq; WP_004531971.1; NZ_LXDZ01000044.1.
DR   KEGG; but:X994_1721; -.
DR   PATRIC; fig|28450.134.peg.3563; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   KO; K01595; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946757};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AIO86419.1}.
FT   ACT_SITE    204    204       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    646    646       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   994 AA;  108834 MW;  E06C0326E873DD34 CRC64;
     MKSSGSARAT RRNAVSSSSA PAHAEPPARR AAKPARKLDG AAARPLAPTN AASAKPQGRT
     REDKDRPLFE DIRYLGRLLG DVVREQEGDA VFDVVETIRQ TAVKFRREDD KAAAQTLEKM
     LRKLTPEQTV SVVRAFSYFS HLANIAEDRH HNRRRRIHAL AGSAAQAGTV AYALDKLKQA
     GDASSKTIKQ FFEGALIVPV LTAHPTEVQR KSILDAQHDI ARLLAERDQP LTARELAHNE
     ALLRARVTTL WQTRMLRDAR LTVADEIENA LSYYRATFLD ELPALYADIE EALAEHGLRA
     RVPAFFQMGS WIGGDRDGNP NVTAATLDEA ISRQAAVIFE HYLEQVHKLG AELSVSNLLV
     GASDALKALA AASPDQSPHR VDEPYRRALI GVYTRLAASA RVRLGEGTVP VRSAGRGAAP
     VRATPYADAE EFAADLRVLT DSLALHHGES LATPRLAPLM RAAEVFGFHL ASIDLRQSSD
     IHEAVVAELL ARGGVEADYA ALPEADKLRV LLAALADPRP LRSPYLDYSD LAKSELGVLE
     RAHAIRAQFG ARAVRNYIIS HTETVSDLVE VLLLQKETGL FEGTLGTPHA NARNGLMVIP
     LFETIADLRN ASDIMRAFFA LPGVGELLAH QGHEQEVMLG YSDSNKDGGF LTSNWELYRA
     ELALVDLFDE RRIKLRLFHG RGGTVGRGGG PTYQAILSQP PGTVNGQIRL TEQGEVIASK
     FANPEIGRRN LETVVAATLE ATLAPHSNAP KQLPAFEAAM QTLSDAAMAS YRALVYETPG
     FTDYFFSSTP ITEIAELNIG SRPASRKLQD PKNRKIEDLR AIPWGFSWGQ CRLLLTGWYG
     FGSAVAAYLD GAPDAAERGK RVALLKKMNK TWPFFANLLS NMDMVLAKTD LAVASRYAQL
     VADKKLRKHV FERIVAEWHR TADALAEITG AHARLAANPL LARSIKNRFP YLDPLNHLQV
     ELIKRHRAGD TNARLRRGIH LTINGIAAGL RNTG
//
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